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Yorodumi- PDB-2c4h: Torpedo californica acetylcholinesterase in complex with 500mM ac... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2c4h | |||||||||
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Title | Torpedo californica acetylcholinesterase in complex with 500mM acetylthiocholine | |||||||||
Components | ACETYLCHOLINESTERASE | |||||||||
Keywords | HYDROLASE / SERINE ESTERASE / SYNAPSE / MEMBRANE / NEUROTRANSMITTER CLEAVAGE / ALPHA/BETA HYDROLASE / SUBSTRATE- INHIBITION / ALTERNATIVE SPLICING / GLYCOPROTEIN / GPI-ANCHOR / LIPOPROTEIN / NEUROTRANSMITTER DEGRADATION | |||||||||
Function / homology | Function and homology information acetylcholine catabolic process in synaptic cleft / acetylcholinesterase / acetylcholinesterase activity / synaptic cleft / side of membrane / synapse / plasma membrane Similarity search - Function | |||||||||
Biological species | TORPEDO CALIFORNICA (Pacific electric ray) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å | |||||||||
Authors | Colletier, J.P. / Fournier, D. / Greenblatt, H.M. / Sussman, J.L. / Zaccai, G. / Silman, I. / Weik, M. | |||||||||
Citation | Journal: EMBO J. / Year: 2006 Title: Structural insights into substrate traffic and inhibition in acetylcholinesterase. Authors: Colletier, J.P. / Fournier, D. / Greenblatt, H.M. / Stojan, J. / Sussman, J.L. / Zaccai, G. / Silman, I. / Weik, M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2c4h.cif.gz | 152.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2c4h.ent.gz | 118.5 KB | Display | PDB format |
PDBx/mmJSON format | 2c4h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c4/2c4h ftp://data.pdbj.org/pub/pdb/validation_reports/c4/2c4h | HTTPS FTP |
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-Related structure data
Related structure data | 2c58C 2c5fC 2c5gC 1ea5S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein / Sugars , 2 types, 3 molecules A
#1: Protein | Mass: 60736.516 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) TORPEDO CALIFORNICA (Pacific electric ray) Organ: ELECTRIC ORGAN / Variant: G2 FORM / Tissue: ELECTROPLAQUE / References: UniProt: P04058, acetylcholinesterase |
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#2: Sugar |
-Non-polymers , 6 types, 965 molecules
#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-ACE / | #6: Chemical | ChemComp-CL / #7: Chemical | ChemComp-ACT / | #8: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.8 Å3/Da / Density % sol: 68 % |
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Crystal grow | Temperature: 277 K / pH: 6 Details: 32% PEG200, 150MM MES, PH6, 4 DEG. C. THE CRYSTAL WAS SOAKED IN A 1.5ML MOTHER LIQUOR SOLUTION CONTAINING 500MM OF THE SUBSTRATE ACETYLTHIOCHOLINE, 40 MINUTES PRIOR TO DATA COLLECTION, pH 6.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97564 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 28, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97564 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→20 Å / Num. obs: 54312 / % possible obs: 99.6 % / Observed criterion σ(I): 3 / Redundancy: 7.34 % / Biso Wilson estimate: 27.9 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 22.14 |
Reflection shell | Resolution: 2.15→2.2 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 3.1 / % possible all: 98.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1EA5 Resolution: 2.15→19.8 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 3357613.85 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 99.5461 Å2 / ksol: 0.343725 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.15→19.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.19 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 20
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Xplor file |
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